Component
The self-hydroxylated Phe300 pterin-stacking residue of tyrosine hydroxylase
The self-hydroxylated Phe300 pterin-stacking residue of tyrosine hydroxylase. Species, exposure and limitations are retained in each linked claim.
1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
Where it participates (unsigned role)
The pterin binds in the active-site cleft forming an aromatic stacking interaction with Phe300, which is itself hydroxylated in the meta position by an autocatalytic process and anchored by a hydrogen bond to the carbonyl of Gln310; the iron sits 5.6 angstrom from the pterin 4a carbon, and molecular oxygen could bind in a bridging position between the pterin and the iron before substrate hydroxylation.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/cold-research/9753429.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3c76ec6d5dadb463c0a044175d5a78fbd02df4da7c339029c8c232e8878175b9", "start_char": 0, "end_char": 1695, "text_sha256": "3c76ec6d5dadb463c0a044175d5a78fbd02df4da7c339029c8c232e8878175b9"}
- experimental_model
- Crystal structure of rat tyrosine hydroxylase with a cofactor analogue and iron at 2.3 angstrom
- exposure
- Bound 7,8-dihydrobiopterin and iron
- limitations
- Structural chemistry of the rate-limiting step. It is a rat enzyme structure with a cofactor analogue, not a measurement of iron status in an animal.
- nutrient_topic
- Cold water immersion research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Cold water immersion
- organism
- Rat enzyme
- plain_language
- The oxygen molecule slots into the gap between the cofactor and the iron.
- primary_references
- [cold-p9753429] Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 A resolution: self-hydroxylation of Phe300 and the pterin-binding site. (1998). https://pubmed.ncbi.nlm.nih.gov/9753429/ DOI: 10.1021/bi981462g
- tissue_or_cell_type
- Purified catalytic and tetramerization domains
Cold water immersion: cold sensing, heat production, the catecholamine axis and what repeated exposure changes (2026-09-19) · lines 546–557
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystal structure of rat tyrosine hydroxylase with a cofactor analogue and iron at 2.3 angstrom · source_derived_draft · unverified_draft
### cold-th-pterin-geometry The pterin binds in the active-site cleft forming an aromatic stacking interaction with Phe300, which is itself hydroxylated in the meta position by an autocatalytic process and anchored by a hydrogen bond to the carbonyl of Gln310; the iron sits 5.6 angstrom from the pterin 4a carbon, and molecular oxygen could bind in a bridging position between the pterin and the iron before substrate hydroxylation. Condition category: normal nutrient_topic: Cold water immersion research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: The oxygen molecule slots into the gap between the cofactor and the iron. organism: Rat enzyme tissue_or_cell_type: Purified catalytic and tetramerization domains experimental_model: Crystal structure of rat tyrosine hydroxylase with a cofactor analogue and iron at 2.3 angstrom limitations: Structural chemistry of the rate-limiting step. It is a rat enzyme structure with a cofactor analogue, not a measurement of iron status in an animal. exposure: Bound 7,8-dihydrobiopterin and iron evidence_span: {"source_cache": "artifacts/cold-research/9753429.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3c76ec6d5dadb463c0a044175d5a78fbd02df4da7c339029c8c232e8878175b9", "start_char": 0, "end_char": 1695, "text_sha256": "3c76ec6d5dadb463c0a044175d5a78fbd02df4da7c339029c8c232e8878175b9"} [cold-p9753429] Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 A resolution: self-hydroxylation of Phe300 and the pterin-binding site. (1998). https://pubmed.ncbi.nlm.nih.gov/9753429/ DOI: 10.1021/bi981462g
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.